|PROSITE documentation PDOC50221 [for PROSITE entry PS50221]|
The GPS domain is a cysteine-rich domain of about 75 amino acid, which was identified in a number of G-protein-coupled receptors (GPCRs) including CIRLs/ latrophilins and in other membrane-associated proteins like the sea urchin receptor for egg jelly protein (REJ). The GPS domain is located immediately N-terminal to transmembrane region (TMRs). For the CIRL-1, CIRL-2, CIRL-3 and CD-97 proteins, it has been shown that they are each made of two non-covalently bound subunits resulting from the endogenous proteolytic cleavage of a precursor protein. Because the cysteine-rich domain of CIRL-1 and possibly other receptors is involved in the endogenous proteolytic processing of CIRL-1 and possibly other receptors, it has been named GPS for GPCR proteolytic site. As the amino acids surrounding the putative cleavage site are the most conserved residues in the GPS domain, it has been suggested that all proteins containing it may be cleaved at this position [1,2,3].
Some proteins known to contain a GPS domain are listed below:
The profile we have developed covers the entire GPS domain.Last update:
December 2001 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Ichtchenko K. Bittner M.A. Krasnoperov V. Little A.R. Chepurny O. Holz R.W. Petrenko A.G.|
|Title||A novel ubiquitously expressed alpha-latrotoxin receptor is a member of the CIRL family of G-protein-coupled receptors.|
|Source||J. Biol. Chem. 274:5491-5498(1999).|
|2||Authors||Sugita S. Ichtchenko K. Khvotchev M. Suedhof T.C.|
|Title||alpha-Latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an unusual family of ubiquitous G-protein-linked receptors. G-protein coupling not required for triggering exocytosis.|
|Source||J. Biol. Chem. 273:32715-32724(1998).|
|3||Authors||Ponting C.P. Hofmann K. Bork P.|
|Title||A latrophilin/CL-1-like GPS domain in polycystin-1.|
|Source||Curr. Biol. 9:R585-R588(1999).|